ID   3L2A2_ACAAN             Reviewed;          35 AA.
AC   P86522;
DT   13-JUL-2010, integrated into UniProtKB/Swiss-Prot.
DT   13-JUL-2010, sequence version 1.
DT   25-MAY-2022, entry version 27.
DE   RecName: Full=Alpha-elapitoxin-Aa2a;
DE            Short=Alpha-EPTX-Aa2a;
DE   Flags: Fragment;
OS   Acanthophis antarcticus (Common death adder).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Serpentes; Colubroidea; Elapidae; Acanthophiinae; Acanthophis.
OX   NCBI_TaxID=8605;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   MASS SPECTROMETRY.
RC   STRAIN=New South Wales; TISSUE=Venom;
RX   PubMed=20950587; DOI=10.1016/j.bcp.2010.10.004;
RA   Blacklow B., Kornhauser R., Hains P.G., Loiacono R., Escoubas P.,
RA   Graudins A., Nicholson G.M.;
RT   "alpha-Elapitoxin-Aa2a, a long-chain snake alpha-neurotoxin with potent
RT   actions on muscle (alpha1)(2)betagammadelta nicotinic receptors, lacks the
RT   classical high affinity for neuronal alpha7 nicotinic receptors.";
RL   Biochem. Pharmacol. 81:314-325(2011).
CC   -!- FUNCTION: Binds to muscular nicotinic acetylcholine receptor (nAChR)
CC       and inhibits acetylcholine from binding to the receptor, thereby
CC       potently impairing neuromuscular transmission. Pseudo-irreversibly
CC       inhibits the nAChR through competitive antagonism. In contrast to other
CC       long-chain alpha-neurotoxins, lacks affinity for neuronal alpha-7
CC       nicotinic acetylcholine receptor. {ECO:0000269|PubMed:20950587}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20950587}.
CC   -!- TISSUE SPECIFICITY: Expressed by the venom gland.
CC       {ECO:0000269|PubMed:20950587}.
CC   -!- MASS SPECTROMETRY: Mass=8850.0; Method=Electrospray;
CC       Evidence={ECO:0000269|PubMed:20950587};
CC   -!- SIMILARITY: Belongs to the snake three-finger toxin family. Long-chain
CC       subfamily. Type II alpha-neurotoxin sub-subfamily. {ECO:0000305}.
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DR   AlphaFoldDB; P86522; -.
DR   SMR; P86522; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0030550; F:acetylcholine receptor inhibitor activity; IEA:UniProtKB-KW.
DR   GO; GO:0099106; F:ion channel regulator activity; IEA:UniProtKB-KW.
DR   GO; GO:0090729; F:toxin activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.10.60.10; -; 1.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   SUPFAM; SSF57302; SSF57302; 1.
PE   1: Evidence at protein level;
KW   Acetylcholine receptor inhibiting toxin; Direct protein sequencing;
KW   Disulfide bond; Ion channel impairing toxin; Neurotoxin;
KW   Postsynaptic neurotoxin; Secreted; Toxin.
FT   CHAIN           1..>35
FT                   /note="Alpha-elapitoxin-Aa2a"
FT                   /id="PRO_0000395310"
FT   DISULFID        3..20
FT                   /evidence="ECO:0000250|UniProtKB:P01386"
FT   DISULFID        13..?
FT                   /evidence="ECO:0000250|UniProtKB:P01386"
FT   DISULFID        26..30
FT                   /evidence="ECO:0000250|UniProtKB:P01386"
FT   NON_TER         35
SQ   SEQUENCE   35 AA;  4049 MW;  5097CDB489310315 CRC64;
     VICYRGYNYA QPCPPGENVC FTKTWCDARC YQLGK